Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O44049 (O44049_TRYRA) Unreviewed, UniProtKB/TrEMBL

Last modified October 16, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
EC=3.2.1.18 EMBL AAC95493.1
OrganismTrypanosoma rangeli EMBL AAC95493.1
Taxonomic identifier5698 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaHerpetosoma

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential EMBL AAC95493.1
Chain23 – 660638sialidase EMBL AAC95493.1
PRO_5000145206

Regions

Region246 – 2494Sulfate 2 binding PDB 1N1V PDB 2FHR PDB 2AGS PDB 2A75 PDB 1N1T
Region614 – 6152Sulfate 3 binding PDB 1N1V PDB 2FHR PDB 2AGS PDB 2A75 PDB 1N1T

Sites

Binding site581Sulfate 1 PDB 1N1S
Binding site2681Sulfate 1 PDB 1N1S
Binding site3371Sulfate 1 PDB 1N1S
Binding site3651Sulfate 1 PDB 1N1S
Binding site4911Sulfate 3 PDB 1N1V PDB 2FHR PDB 2AGS PDB 2A75 PDB 1N1T

Amino acid modifications

Glycosylation371N-linked (GlcNAc...) PDB 1MZ6 PDB 1MZ5
Glycosylation461N-linked (GlcNAc...) PDB 1MZ6 PDB 1MZ5
Glycosylation1371N-linked (GlcNAc...) PDB 1MZ6 PDB 1MZ5
Glycosylation4511N-linked (GlcNAc...) PDB 1MZ6 PDB 1MZ5
Glycosylation6361N-linked (GlcNAc...) PDB 1MZ6 PDB 1MZ5

Sequences

Sequence LengthMass (Da)Tools
O44049 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: B5D55765DC4423D0

FASTA66071,965
        10         20         30         40         50         60 
MSWLAVFVPL FLMACASEPA SALAPGSSRV ELFKRKNSTV PFEESNGTIR ERVVHSFRIP 

        70         80         90        100        110        120 
TIVNVDGVMV ATADARYETS FDNSFIETAV KYSVDDGATW NTQIAIKNSR ASSVSRVMDA 

       130        140        150        160        170        180 
TVIVKGNKLY ILVGSFNKTR NSWTQHRDGS DWEPLLVVGE VTKSAANGKT TATISWGKPV 

       190        200        210        220        230        240 
SLKPLFPAEF DGILTKEFIG GVGAAIVGSN GNLVYPVQIA DMGGRVFTKI MYSEDDGNTW 

       250        260        270        280        290        300 
KFAEGRSKFG CSEPAVLEWE GKLIINNRVD GNRRLVYESS DMGKTWVEAL GTLSHVWTNS 

       310        320        330        340        350        360 
PTSNQQDCQS SFVAVTIEGK RVMLFTHPLN LKGRWMRDRL HLWMTDNQRI FDVGQISIGD 

       370        380        390        400        410        420 
ENSGYSSVLY KDDKLYSLHE INTNDVYSLV FVRFIGELQL MKSVVRTWKE EDNHLASICT 

       430        440        450        460        470        480 
PVVPATPPSK GGCGAAVPTA GLVGFLSHSA NGSVWEDVYR CVDANVANAE RVPNGLKFNG 

       490        500        510        520        530        540 
VGGGAVWPVA RQGQTRRYQF ANYRFTLVAT VTIDELPKGT SPLLGAGLEG PGDAKLLGLS 

       550        560        570        580        590        600 
YDKNRQWRPL YGAAPASPTG SWELHKKYHV VLTMADRQGS VYVDGQPLAG SGNTVVRGAT 

       610        620        630        640        650        660 
LPDISHFYIG GPRSKGAPTD SRVTVTNIVL YNRRLNSSEI RTLFLSQDMI GTDGGAGTAA 

« Hide

References

[1]"Trypanosoma rangeli sialidase: cloning, expression and similarity to T. cruzi trans-sialidase."
Buschiazzo A., Campetella O., Frasch A.C.
Glycobiology 7:1167-1173(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: LDG EMBL AAC95493.1.
[2]"Structural basis of sialyltransferase activity in trypanosomal sialidases."
Buschiazzo A., Tavares G.A., Campetella O., Spinelli S., Cremona M.L., Paris G., Amaya M.F., Frasch A.C., Alzari P.M.
EMBO J. 19:16-24(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-660, GLYCOSYLATION AT ASN-37; ASN-46; ASN-137; ASN-451 AND ASN-636.
[3]"The high resolution structures of free and inhibitor-bound Trypanosoma rangeli sialidase and its comparison with T. cruzi trans-sialidase."
Amaya M.F., Buschiazzo A., Nguyen T., Alzari P.M.
J. Mol. Biol. 325:773-784(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 23-660 IN COMPLEX WITH SULFATE.
[4]"A sialidase mutant displaying trans-sialidase activity."
Paris G., Ratier L., Amaya M.F., Nguyen T., Alzari P.M., Frasch A.C.
J. Mol. Biol. 345:923-934(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 23-660.
[5]"Structural and kinetic analysis of two covalent sialosyl-enzyme intermediates on Trypanosoma rangeli sialidase."
Watts A.G., Oppezzo P., Withers S.G., Alzari P.M., Buschiazzo A.
J. Biol. Chem. 281:4149-4155(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 23-660 IN COMPLEX WITH SULFATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U83180 Genomic DNA. Translation: AAC95493.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZ5X-ray2.20A23-660[»]
1MZ6X-ray2.90A23-660[»]
1N1SX-ray1.64A23-660[»]
1N1TX-ray1.60A23-660[»]
1N1VX-ray2.10A23-660[»]
1N1YX-ray2.80A23-660[»]
1WCSX-ray2.80A23-660[»]
2A75X-ray1.95A23-660[»]
2AGSX-ray1.70A23-660[»]
2FHRX-ray2.20A23-660[»]
ProteinModelPortalO44049.
SMRO44049. Positions 21-653.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.120.10.10. 1 hit.
2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR026948. Sialidase/anhydrosialidase.
IPR026856. Sialidase_fam.
IPR008377. Sialidase_trypan.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF5. PTHR10628:SF5. 1 hit.
PRINTSPR01803. TCSIALIDASE.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO44049.

Entry information

Entry nameO44049_TRYRA
AccessionPrimary (citable) accession number: O44049
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: October 16, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)